RL29_HALMA
ID RL29_HALMA Reviewed; 71 AA.
AC P10971; P22526; Q5V1T1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=50S ribosomal protein L29;
DE AltName: Full=Hl33;
DE AltName: Full=Hmal29;
GN Name=rpl29; OrderedLocusNames=rrnAC1604;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7;
RA Arndt E., Kroemer W., Hatakeyama T.;
RT "Organization and nucleotide sequence of a gene cluster coding for eight
RT ribosomal proteins in the archaebacterium Halobacterium marismortui.";
RL J. Biol. Chem. 265:3034-3039(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-70.
RX PubMed=3191994; DOI=10.1016/0014-5793(88)80333-8;
RA Hatakeyama T., Hatakeyama T., Kimura M.;
RT "The primary structures of ribosomal proteins L16, L23 and L33 from the
RT archaebacterium Halobacterium marismortui.";
RL FEBS Lett. 240:21-28(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-71.
RX PubMed=2143141; DOI=10.1016/0014-5793(90)80923-7;
RA Arndt E.;
RT "Nucleotide sequence of four genes encoding ribosomal proteins from the
RT 'S10 and spectinomycin' operon equivalent region in the archaebacterium
RT Halobacterium marismortui.";
RL FEBS Lett. 267:193-198(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937989; DOI=10.1126/science.289.5481.905;
RA Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.;
RT "The complete atomic structure of the large ribosomal subunit at 2.4 A
RT resolution.";
RL Science 289:905-920(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937990; DOI=10.1126/science.289.5481.920;
RA Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.;
RT "The structural basis of ribosome activity in peptide bond synthesis.";
RL Science 289:920-930(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11828326; DOI=10.1038/nsb758;
RA Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K.,
RA Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.;
RT "A pre-translocational intermediate in protein synthesis observed in
RT crystals of enzymatically active 50S subunits.";
RL Nat. Struct. Biol. 9:225-230(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11483524; DOI=10.1093/emboj/20.15.4214;
RA Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "The kink-turn: a new RNA secondary structure motif.";
RL EMBO J. 20:4214-4221(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FOUR MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1;
RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.;
RT "The structures of four macrolide antibiotics bound to the large ribosomal
RT subunit.";
RL Mol. Cell 10:117-128(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12185246; DOI=10.1073/pnas.172404099;
RA Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structural insights into peptide bond formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12860128; DOI=10.1016/s0022-2836(03)00668-5;
RA Hansen J.L., Moore P.B., Steitz T.A.;
RT "Structures of five antibiotics bound at the peptidyl transferase center of
RT the large ribosomal subunit.";
RL J. Mol. Biol. 330:1061-1075(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT
RP E SITE SUBSTRATES.
RX PubMed=14561884; DOI=10.1261/rna.5120503;
RA Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structures of deacylated tRNA mimics bound to the E site of the large
RT ribosomal subunit.";
RL RNA 9:1345-1352(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RX PubMed=23695244; DOI=10.1107/s0907444913004745;
RA Gabdulkhakov A., Nikonov S., Garber M.;
RT "Revisiting the Haloarcula marismortui 50S ribosomal subunit model.";
RL Acta Crystallogr. D 69:997-1004(2013).
CC -!- FUNCTION: Stabilizes the tertiary rRNA structure within the 23S rRNA
CC domain (domain I) to which it binds. Located at the polypeptide exit
CC tunnel on the outside of the subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein L23.
CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC {ECO:0000305}.
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DR EMBL; J05222; AAA86866.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46521.1; -; Genomic_DNA.
DR EMBL; X55311; CAA39015.1; -; Genomic_DNA.
DR PIR; A35064; R5HS29.
DR PIR; T46794; T46794.
DR RefSeq; WP_004516964.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; S=2-71.
DR PDB; 1JJ2; X-ray; 2.40 A; U=2-71.
DR PDB; 1K73; X-ray; 3.01 A; W=2-71.
DR PDB; 1K8A; X-ray; 3.00 A; W=2-71.
DR PDB; 1K9M; X-ray; 3.00 A; W=2-71.
DR PDB; 1KC8; X-ray; 3.01 A; W=2-71.
DR PDB; 1KD1; X-ray; 3.00 A; W=2-71.
DR PDB; 1KQS; X-ray; 3.10 A; U=2-71.
DR PDB; 1M1K; X-ray; 3.20 A; W=2-71.
DR PDB; 1M90; X-ray; 2.80 A; W=2-71.
DR PDB; 1ML5; EM; 14.00 A; w=2-71.
DR PDB; 1N8R; X-ray; 3.00 A; W=2-71.
DR PDB; 1NJI; X-ray; 3.00 A; W=2-71.
DR PDB; 1Q7Y; X-ray; 3.20 A; W=2-71.
DR PDB; 1Q81; X-ray; 2.95 A; W=2-71.
DR PDB; 1Q82; X-ray; 2.98 A; W=2-71.
DR PDB; 1Q86; X-ray; 3.00 A; W=2-71.
DR PDB; 1QVF; X-ray; 3.10 A; U=2-71.
DR PDB; 1QVG; X-ray; 2.90 A; U=2-71.
DR PDB; 1S72; X-ray; 2.40 A; V=1-71.
DR PDB; 1VQ4; X-ray; 2.70 A; V=1-71.
DR PDB; 1VQ5; X-ray; 2.60 A; V=1-71.
DR PDB; 1VQ6; X-ray; 2.70 A; V=1-71.
DR PDB; 1VQ7; X-ray; 2.50 A; V=1-71.
DR PDB; 1VQ8; X-ray; 2.20 A; V=1-71.
DR PDB; 1VQ9; X-ray; 2.40 A; V=1-71.
DR PDB; 1VQK; X-ray; 2.30 A; V=1-71.
DR PDB; 1VQL; X-ray; 2.30 A; V=1-71.
DR PDB; 1VQM; X-ray; 2.30 A; V=1-71.
DR PDB; 1VQN; X-ray; 2.40 A; V=1-71.
DR PDB; 1VQO; X-ray; 2.20 A; V=1-71.
DR PDB; 1VQP; X-ray; 2.25 A; V=1-71.
DR PDB; 1W2B; X-ray; 3.50 A; U=2-71.
DR PDB; 1YHQ; X-ray; 2.40 A; V=1-71.
DR PDB; 1YI2; X-ray; 2.65 A; V=1-71.
DR PDB; 1YIJ; X-ray; 2.60 A; V=1-71.
DR PDB; 1YIT; X-ray; 2.80 A; V=1-71.
DR PDB; 1YJ9; X-ray; 2.90 A; V=1-71.
DR PDB; 1YJN; X-ray; 3.00 A; V=1-71.
DR PDB; 1YJW; X-ray; 2.90 A; V=1-71.
DR PDB; 2OTJ; X-ray; 2.90 A; V=1-71.
DR PDB; 2OTL; X-ray; 2.70 A; V=1-71.
DR PDB; 2QA4; X-ray; 3.00 A; V=1-71.
DR PDB; 2QEX; X-ray; 2.90 A; V=1-71.
DR PDB; 3CC2; X-ray; 2.40 A; V=1-71.
DR PDB; 3CC4; X-ray; 2.70 A; V=1-71.
DR PDB; 3CC7; X-ray; 2.70 A; V=1-71.
DR PDB; 3CCE; X-ray; 2.75 A; V=1-71.
DR PDB; 3CCJ; X-ray; 2.70 A; V=1-71.
DR PDB; 3CCL; X-ray; 2.90 A; V=1-71.
DR PDB; 3CCM; X-ray; 2.55 A; V=1-71.
DR PDB; 3CCQ; X-ray; 2.90 A; V=1-71.
DR PDB; 3CCR; X-ray; 3.00 A; V=1-71.
DR PDB; 3CCS; X-ray; 2.95 A; V=1-71.
DR PDB; 3CCU; X-ray; 2.80 A; V=1-71.
DR PDB; 3CCV; X-ray; 2.90 A; V=1-71.
DR PDB; 3CD6; X-ray; 2.75 A; V=1-71.
DR PDB; 3CMA; X-ray; 2.80 A; V=1-71.
DR PDB; 3CME; X-ray; 2.95 A; V=1-71.
DR PDB; 3CPW; X-ray; 2.70 A; U=1-71.
DR PDB; 3CXC; X-ray; 3.00 A; U=2-71.
DR PDB; 3G4S; X-ray; 3.20 A; V=2-66.
DR PDB; 3G6E; X-ray; 2.70 A; V=2-66.
DR PDB; 3G71; X-ray; 2.85 A; V=2-66.
DR PDB; 3I55; X-ray; 3.11 A; V=1-71.
DR PDB; 3I56; X-ray; 2.90 A; V=1-71.
DR PDB; 3OW2; X-ray; 2.70 A; U=2-66.
DR PDB; 4ADX; EM; 6.60 A; V=1-71.
DR PDB; 4V42; X-ray; 5.50 A; BW=2-71.
DR PDB; 4V4R; X-ray; 5.90 A; 2=2-71.
DR PDB; 4V4S; X-ray; 6.76 A; 2=2-71.
DR PDB; 4V4T; X-ray; 6.46 A; 2=2-71.
DR PDB; 4V9F; X-ray; 2.40 A; V=1-71.
DR PDBsum; 1FFK; -.
DR PDBsum; 1JJ2; -.
DR PDBsum; 1K73; -.
DR PDBsum; 1K8A; -.
DR PDBsum; 1K9M; -.
DR PDBsum; 1KC8; -.
DR PDBsum; 1KD1; -.
DR PDBsum; 1KQS; -.
DR PDBsum; 1M1K; -.
DR PDBsum; 1M90; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 1N8R; -.
DR PDBsum; 1NJI; -.
DR PDBsum; 1Q7Y; -.
DR PDBsum; 1Q81; -.
DR PDBsum; 1Q82; -.
DR PDBsum; 1Q86; -.
DR PDBsum; 1QVF; -.
DR PDBsum; 1QVG; -.
DR PDBsum; 1S72; -.
DR PDBsum; 1VQ4; -.
DR PDBsum; 1VQ5; -.
DR PDBsum; 1VQ6; -.
DR PDBsum; 1VQ7; -.
DR PDBsum; 1VQ8; -.
DR PDBsum; 1VQ9; -.
DR PDBsum; 1VQK; -.
DR PDBsum; 1VQL; -.
DR PDBsum; 1VQM; -.
DR PDBsum; 1VQN; -.
DR PDBsum; 1VQO; -.
DR PDBsum; 1VQP; -.
DR PDBsum; 1W2B; -.
DR PDBsum; 1YHQ; -.
DR PDBsum; 1YI2; -.
DR PDBsum; 1YIJ; -.
DR PDBsum; 1YIT; -.
DR PDBsum; 1YJ9; -.
DR PDBsum; 1YJN; -.
DR PDBsum; 1YJW; -.
DR PDBsum; 2OTJ; -.
DR PDBsum; 2OTL; -.
DR PDBsum; 2QA4; -.
DR PDBsum; 2QEX; -.
DR PDBsum; 3CC2; -.
DR PDBsum; 3CC4; -.
DR PDBsum; 3CC7; -.
DR PDBsum; 3CCE; -.
DR PDBsum; 3CCJ; -.
DR PDBsum; 3CCL; -.
DR PDBsum; 3CCM; -.
DR PDBsum; 3CCQ; -.
DR PDBsum; 3CCR; -.
DR PDBsum; 3CCS; -.
DR PDBsum; 3CCU; -.
DR PDBsum; 3CCV; -.
DR PDBsum; 3CD6; -.
DR PDBsum; 3CMA; -.
DR PDBsum; 3CME; -.
DR PDBsum; 3CPW; -.
DR PDBsum; 3CXC; -.
DR PDBsum; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 3OW2; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V42; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P10971; -.
DR SMR; P10971; -.
DR IntAct; P10971; 3.
DR STRING; 272569.rrnAC1604; -.
DR EnsemblBacteria; AAV46521; AAV46521; rrnAC1604.
DR GeneID; 40152570; -.
DR GeneID; 64821822; -.
DR KEGG; hma:rrnAC1604; -.
DR PATRIC; fig|272569.17.peg.2294; -.
DR eggNOG; arCOG00785; Archaea.
DR HOGENOM; CLU_158491_2_2_2; -.
DR OMA; ELRDMTP; -.
DR EvolutionaryTrace; P10971; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.310; -; 1.
DR HAMAP; MF_00374; Ribosomal_L29; 1.
DR InterPro; IPR001854; Ribosomal_L29/L35.
DR InterPro; IPR036049; Ribosomal_L29/L35_sf.
DR InterPro; IPR018254; Ribosomal_L29_CS.
DR Pfam; PF00831; Ribosomal_L29; 1.
DR SUPFAM; SSF46561; SSF46561; 1.
DR TIGRFAMs; TIGR00012; L29; 1.
DR PROSITE; PS00579; RIBOSOMAL_L29; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3191994"
FT CHAIN 2..71
FT /note="50S ribosomal protein L29"
FT /id="PRO_0000130508"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 14..36
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 44..64
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 71 AA; 7879 MW; 31779CA339CC699A CRC64;
MTVLHVQEIR DMTPAEREAE LDDLKTELLN ARAVQAAGGA PENPGRIKEL RKAIARIKTI
QGEEGDLQEN E
